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1lki

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(New page: 200px<br /><applet load="1lki" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lki, resolution 2.0&Aring;" /> '''THE CRYSTAL STRUCTURE...)
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caption="1lki, resolution 2.0&Aring;" />
'''THE CRYSTAL STRUCTURE AND BIOLOGICAL FUNCTION OF LEUKEMIA INHIBITORY FACTOR: IMPLICATIONS FOR RECEPTOR BINDING'''<br />
'''THE CRYSTAL STRUCTURE AND BIOLOGICAL FUNCTION OF LEUKEMIA INHIBITORY FACTOR: IMPLICATIONS FOR RECEPTOR BINDING'''<br />
==Overview==
==Overview==
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The structure of murine leukemia inhibitory factor (LIF) has been, determined by X-ray crystallography at 2.0 A resolution. The main chain, fold conforms to the four alpha-helix bundle topology previously observed, for several members of the hematopoietic cytokine family. Of these, LIF, shows closest structural homology to granulocyte colony-stimulating factor, and growth hormone (GH). Sequence alignments for the functionally related, molecules oncostatin M and ciliary neurotrophic factor, when mapped to the, LIF structure, indicate regions of conserved surface character. Analysis, of the biological function and receptor specificity of a series of, human-mouse LIF chimeras implicate two regions of receptor interaction, that are located in the fourth helix and the preceding loop. A model for, receptor binding based on the structure of the GH ligand-receptor complex, requires additional, novel features to account for these data.
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The structure of murine leukemia inhibitory factor (LIF) has been determined by X-ray crystallography at 2.0 A resolution. The main chain fold conforms to the four alpha-helix bundle topology previously observed for several members of the hematopoietic cytokine family. Of these, LIF shows closest structural homology to granulocyte colony-stimulating factor and growth hormone (GH). Sequence alignments for the functionally related molecules oncostatin M and ciliary neurotrophic factor, when mapped to the LIF structure, indicate regions of conserved surface character. Analysis of the biological function and receptor specificity of a series of human-mouse LIF chimeras implicate two regions of receptor interaction that are located in the fourth helix and the preceding loop. A model for receptor binding based on the structure of the GH ligand-receptor complex requires additional, novel features to account for these data.
==About this Structure==
==About this Structure==
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1LKI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LKI OCA].
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1LKI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LKI OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Grey, L.M.]]
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[[Category: Grey, L M.]]
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[[Category: Heath, J.K.]]
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[[Category: Heath, J K.]]
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[[Category: Jones, E.Y.]]
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[[Category: Jones, E Y.]]
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[[Category: Robinson, R.C.]]
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[[Category: Robinson, R C.]]
[[Category: Staunton, D.]]
[[Category: Staunton, D.]]
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[[Category: Stuart, D.I.]]
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[[Category: Stuart, D I.]]
[[Category: cytokine]]
[[Category: cytokine]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:37:40 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:45:45 2008''

Revision as of 11:45, 21 February 2008

Image:1lki.gif

1lki, resolution 2.0Å

Drag the structure with the mouse to rotate

THE CRYSTAL STRUCTURE AND BIOLOGICAL FUNCTION OF LEUKEMIA INHIBITORY FACTOR: IMPLICATIONS FOR RECEPTOR BINDING

Overview

The structure of murine leukemia inhibitory factor (LIF) has been determined by X-ray crystallography at 2.0 A resolution. The main chain fold conforms to the four alpha-helix bundle topology previously observed for several members of the hematopoietic cytokine family. Of these, LIF shows closest structural homology to granulocyte colony-stimulating factor and growth hormone (GH). Sequence alignments for the functionally related molecules oncostatin M and ciliary neurotrophic factor, when mapped to the LIF structure, indicate regions of conserved surface character. Analysis of the biological function and receptor specificity of a series of human-mouse LIF chimeras implicate two regions of receptor interaction that are located in the fourth helix and the preceding loop. A model for receptor binding based on the structure of the GH ligand-receptor complex requires additional, novel features to account for these data.

About this Structure

1LKI is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

The crystal structure and biological function of leukemia inhibitory factor: implications for receptor binding., Robinson RC, Grey LM, Staunton D, Vankelecom H, Vernallis AB, Moreau JF, Stuart DI, Heath JK, Jones EY, Cell. 1994 Jul 1;77(7):1101-16. PMID:8020098

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